KCTD10 Biology : An Adaptor for the Ubiquitin E3 Complex Meets Multiple Substrates: Emerging Divergent Roles of the cullin-3/KCTD10 E3 Ubiquitin Ligase Complex in Various Cell Lines

© 2020 WILEY Periodicals, Inc..

Protein ubiquitination constitutes a post-translational modification mediated by ubiquitin ligases whereby ubiquitinated substrates are degraded through the proteasomal or lysosomal pathways, or acquire novel molecular functions according to their "ubiquitin codes." Dysfunction of the ubiquitination process in cells causes various diseases such as cancers along with neurodegenerative, auto-immune/inflammatory, and metabolic diseases. KCTD10 functions as a substrate recognition receptor for cullin-3 (CUL3), a scaffold protein in RING-type ubiquitin ligase complexes. Recently, studies by ourselves and others have identified new substrates that are ubiquitinated by the CUL3/KCTD10 ubiquitin ligase complex. Moreover, the type of polyubiquitination (e.g., K27-, K48-, or K63-chain) of various substrates (e.g., RhoB, CEP97, EIF3D, and TRIF) mediated by KCTD10 underlies its divergent roles in endothelial barrier formation, primary cilium formation, plasma membrane dynamics, cell proliferation, and immune response. Here, the physiological functions of KCTD10 are summarized and potential mechanisms are proposed.

Medienart:

E-Artikel

Erscheinungsjahr:

2020

Erschienen:

2020

Enthalten in:

Zur Gesamtaufnahme - volume:42

Enthalten in:

BioEssays : news and reviews in molecular, cellular and developmental biology - 42(2020), 8 vom: 02. Aug., Seite e1900256

Sprache:

Englisch

Beteiligte Personen:

Maekawa, Masashi [VerfasserIn]
Higashiyama, Shigeki [VerfasserIn]

Links:

Volltext

Themen:

CEP97
Cullin Proteins
Cullin-3
EC 2.3.2.27
EIF3D
EIF3D protein, human
Eukaryotic Initiation Factor-3
Journal Article
KCTD10
KCTD10 protein, human
Potassium Channels, Voltage-Gated
Research Support, Non-U.S. Gov't
RhoB
TRIF
Ubiquitin
Ubiquitin E3 ligase
Ubiquitin-Protein Ligases

Anmerkungen:

Date Completed 18.08.2021

Date Revised 18.08.2021

published: Print-Electronic

Citation Status MEDLINE

doi:

10.1002/bies.201900256

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM310645662